A quantitative, high-throughput screen for protein stability.
about
Monitoring protein stability in vivoExpanding the number of 'druggable' targets: non-enzymes and protein-protein interactionsEvidence of Fe3+ interaction with the plug domain of the outer membrane transferrin receptor protein of Neisseria gonorrhoeae: implications for Fe transportReexamination of the recognition preference of the specificity pocket of the Abl SH3 domain.Hydrogen/deuterium exchange of hydrophobic peptides in model membranes by electrospray ionization mass spectrometry.Imidazole C-2 hydrogen/deuterium exchange reaction at histidine for probing protein structure and function with matrix-assisted laser desorption ionization mass spectrometry.Construct optimization for protein NMR structure analysis using amide hydrogen/deuterium exchange mass spectrometry.A cell is more than the sum of its (dilute) parts: A brief history of quinary structure.A miniaturized technique for assessing protein thermodynamics and function using fast determination of quantitative cysteine reactivity.Tools to evaluate the conformation of protein products.Integrating mass spectrometry of intact protein complexes into structural proteomicsPeptide-column interactions and their influence on back exchange rates in hydrogen/deuterium exchange-MS.Thermodynamic stability measurements on multimeric proteins using a new H/D exchange- and matrix-assisted laser desorption/ionization (MALDI) mass spectrometry-based method.Accuracy of SUPREX (stability of unpurified proteins from rates of H/D exchange) and MALDI mass spectrometry-derived protein unfolding free energies determined under non-EX2 exchange conditions.Throughput and efficiency of a mass spectrometry-based screening assay for protein-ligand binding detection.The calcium-modulated structures of calmodulin and S100b proteins are useful to monitor hydrogen/deuterium exchange efficiency using matrix-assisted laser desorption ionization time-of-flight mass spectrometry.Hydrogen/deuterium exchange- and protease digestion-based screening assay for protein-ligand binding detection.Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity.Thermodynamic analysis of a molecular chaperone binding to unfolded protein substrates.Comparison of Two ESI MS Based H/D Exchange Methods for Extracting Protein Folding Energies.Differential hydrogen/deuterium exchange mass spectrometry analysis of protein-ligand interactionsProtein Footprinting by Carbenes on a Fast Photochemical Oxidation of Proteins (FPOP) Platform.Slow histidine H/D exchange protocol for thermodynamic analysis of protein folding and stability using mass spectrometry.Theory of the Protein Equilibrium Population Snapshot by H/D Exchange Electrospray Ionization Mass Spectrometry (PEPS-HDX-ESI-MS) Method used to obtain Protein Folding Energies/Rates and Selected Supporting Experimental Evidence.Folding and assembly of large macromolecular complexes monitored by hydrogen-deuterium exchange and mass spectrometry.Strong anion exchange for studying protein-DNA interactions by H/D exchange mass spectrometry.Thermodynamic analysis of protein-ligand binding interactions in complex biological mixtures using the stability of proteins from rates of oxidationFalse-positive rate determination of protein target discovery using a covalent modification- and mass spectrometry-based proteomics platform.Unraveling the dynamics of protein interactions with quantitative mass spectrometry.Protein stability by number: high-throughput and statistical approaches to one of protein science's most difficult problems.Painting proteins with covalent labels: what's in the picture?Quantitation of protein-protein interactions by thermal stability shift analysisApplication of Titration-Based Screening for the Rapid Pilot Testing of High-Throughput Assays.Conformational characterization of the charge variants of a human IgG1 monoclonal antibody using H/D exchange mass spectrometry.Analysis of the stability of multimeric proteins by effective DeltaG and effective m-valuesDetermining protein stability in cell lysates by pulse proteolysis and Western blottingComputer-aided NMR assay for detecting natively folded structural domains.In vivo and in vitro examination of stability of primary hyperoxaluria-associated human alanine:glyoxylate aminotransferase.Protein unfolding with a steric trap.ESI-MS and FTIR studies of the interaction between the second PDZ domain of hPTP1E and target peptides.
P2860
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P2860
A quantitative, high-throughput screen for protein stability.
description
2000 nî lūn-bûn
@nan
2000 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
A quantitative, high-throughput screen for protein stability.
@ast
A quantitative, high-throughput screen for protein stability.
@en
type
label
A quantitative, high-throughput screen for protein stability.
@ast
A quantitative, high-throughput screen for protein stability.
@en
prefLabel
A quantitative, high-throughput screen for protein stability.
@ast
A quantitative, high-throughput screen for protein stability.
@en
P2093
P2860
P356
P1476
A quantitative, high-throughput screen for protein stability.
@en
P2093
M C Fitzgerald
S Ghaemmaghami
P2860
P304
P356
10.1073/PNAS.140111397
P407
P577
2000-07-01T00:00:00Z